Table 1.
Data collection | |
---|---|
Resolution (Å) | 50–2.7 |
No. observations | 65,855 |
No. unique | 26,564 |
Redundancy* | 2.8 (2.4) |
% Complete | 92.5 (73.7) |
Rsym† | 0.056 (0.195) |
No. of reflections Rwork (Rfree) | 24,727 (1,322) |
Rwork‡ (Rfree) | 24.2 (29.5) |
rmsd§ bonds (Å) | 0.007 |
rmsd angles (°) | 1.35 |
Overall avg. B-factor (Å2) | 52.3 |
rmsd¶ B (main chain, Å2) | 2.8 |
smsd¶ B (side chain, Å2) | 3.7 |
No. protein atoms | 5,627 |
No. of NAG molecules | 2 |
No. water molecules | 48 |
Ramachandran plot quality | |
Most favored (%) | 83.2 |
Additionally favored (%) | 15.8 |
Generously allowed (%) | 1.0 |
Disallowed (%) | 0.0 |
NAG, N-acetylglucosamine.
Parentheses denote statistics in the highest resolution shell of 2.8–2.7 Å.
Rsym = (Σ|I(i) − 〈I(h)〉|)/(ΣI(i)) where I(i) is the ith observation of the intensity of a reflection with indices h, k, l and 〈I(h)〉 is the average intensity of all symmetry equivalent measurements of that reflection.
Rwork = Σ|Fobs(h) − Fcalc(h)|/Σ|Fobs(h)| where Fobs(h) and Fcalc(h) are the observed and calculated structure factor amplitudes, respectively. Rfree is calculated as Rwork but for 5% of the data excluded from refinement.
rms deviations (rmsd) in bond lengths and angles are the deviations from ideal values.
rmsd for bonded atoms.